دورية أكاديمية
أعرض في EDS

Targeting the interaction of pleiotrophin and VEGFA 165 with protein tyrosine phosphatase receptor zeta 1 inhibits endothelial cell activation and angiogenesis.

التفاصيل البيبلوغرافية
العنوان: Targeting the interaction of pleiotrophin and VEGFA 165 with protein tyrosine phosphatase receptor zeta 1 inhibits endothelial cell activation and angiogenesis.
المؤلفون: Choleva E; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, 26504, Greece., Menounou L; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, 26504, Greece., Ntenekou D; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, 26504, Greece., Kastana P; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, 26504, Greece., Tzoupis Η; Department of Chemistry, University of Patras, Patras, Greece., Katraki-Pavlou S; Zebrafish Disease Models Lab, Center for Clinical, Experimental Surgery and Translational Research, Biomedical Research Foundation Academy of Athens, Greece., Drakopoulou M; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, 26504, Greece., Spyropoulos D; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, 26504, Greece., Andrikopoulou A; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, 26504, Greece., Kanellopoulou V; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, 26504, Greece., Enake MK; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, 26504, Greece., Beis D; Zebrafish Disease Models Lab, Center for Clinical, Experimental Surgery and Translational Research, Biomedical Research Foundation Academy of Athens, Greece; Laboratory of Biological Chemistry, Faculty of Medicine, University of Ioannina, Greece., Papadimitriou E; Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Patras, 26504, Greece. Electronic address: epapad@upatras.gr.
المصدر: European journal of pharmacology [Eur J Pharmacol] 2024 Aug 15; Vol. 977, pp. 176692. Date of Electronic Publication: 2024 May 29.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Science Country of Publication: Netherlands NLM ID: 1254354 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0712 (Electronic) Linking ISSN: 00142999 NLM ISO Abbreviation: Eur J Pharmacol Subsets: MEDLINE
أسماء مطبوعة: Publication: 2005- : Amsterdam : Elsevier Science
Original Publication: Amsterdam, North Holland Pub. Co.
مواضيع طبية MeSH: Vascular Endothelial Growth Factor A*/metabolism , Vascular Endothelial Growth Factor A*/pharmacology , Receptor-Like Protein Tyrosine Phosphatases, Class 5*/metabolism , Cell Movement*/drug effects , Cytokines*/metabolism , Carrier Proteins*/metabolism , Carrier Proteins*/pharmacology , Human Umbilical Vein Endothelial Cells*/drug effects , Neovascularization, Physiologic*/drug effects, Humans ; Animals ; Chick Embryo ; Zebrafish ; Protein Binding ; Cell Proliferation/drug effects ; Cell Line, Tumor ; Endothelial Cells/drug effects ; Endothelial Cells/metabolism ; Neovascularization, Pathologic ; Glioblastoma/pathology ; Glioblastoma/metabolism ; Glioblastoma/drug therapy ; Angiogenesis
مستخلص: Protein tyrosine phosphatase receptor zeta 1 (PTPRZ1) is a transmembrane tyrosine phosphatase (TP) that serves as a receptor for pleiotrophin (PTN) and vascular endothelial growth factor A 165 (VEGFA 165 ) to regulate endothelial cell migration. In the present work, we identify a PTN peptide fragment (PTN 97-110 ) that inhibits the interaction of PTN and VEGFA 165 with PTPRZ1 but not VEGF receptor 2. This peptide abolishes the stimulatory effect of PTN and VEGFA 165 on endothelial cell migration, tube formation on Matrigel, and Akt activation in vitro. It also partially inhibits VEGFA 165 -induced VEGF receptor 2 activation but does not affect ERK1/2 activation and cell proliferation. In vivo, PTN 97-110 inhibits or dysregulates angiogenesis in the chick embryo chorioallantoic membrane and the zebrafish assays, respectively. In glioblastoma cells in vitro, PTN 97-110 abolishes the stimulatory effect of VEGFA 165 on cell migration and inhibits their anchorage-independent growth, suggesting that this peptide might also be exploited in glioblastoma therapy. Finally, in silico and experimental evidence indicates that PTN and VEGFA 165 bind to the extracellular fibronectin type-III (FNIII) domain to stimulate cell migration. Collectively, our data highlight novel aspects of the interaction of PTN and VEGFA 165 with PTPRZ1, strengthen the notion that PTPRZ1 is required for VEGFA 165 -induced signaling, and identify a peptide that targets this interaction and can be exploited for the design of novel anti-angiogenic and anti-glioblastoma therapeutic approaches.
Competing Interests: Declaration of competing interest All authors declare no conflict of interest.
(Copyright © 2024 The Authors. Published by Elsevier B.V. All rights reserved.)
فهرسة مساهمة: Keywords: Angiogenesis inhibition; Endothelial; Glioblastoma; PTPRZ1; Tyrosine phosphatase; VEGFA
المشرفين على المادة: 134034-50-7 (pleiotrophin)
0 (Vascular Endothelial Growth Factor A)
EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 5)
0 (Cytokines)
0 (Carrier Proteins)
0 (VEGFA protein, human)
EC 3.1.3.48 (PTPRZ1 protein, human)
تواريخ الأحداث: Date Created: 20240531 Date Completed: 20240701 Latest Revision: 20240701
رمز التحديث: 20240702
DOI: 10.1016/j.ejphar.2024.176692
PMID: 38821164
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-0712
DOI:10.1016/j.ejphar.2024.176692